Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste
L-methioninase is an enzyme that has recently gained significant interest in the scientific community because of its potential as a targeted therapy for cancer. This study aims to isolate and identify extremophilic bacteria that could produce L-methioninase and to access the enzymatic potential of i...
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MDPI AG
2023-07-01
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| Series: | Microbiology Research |
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| author | Bhumi Javia Megha Gadhvi Suhas Vyas Pravin Dudhagara Douglas J. H. Shyu Yih-Yuan Chen Dushyant Dudhagara |
| author_facet | Bhumi Javia Megha Gadhvi Suhas Vyas Pravin Dudhagara Douglas J. H. Shyu Yih-Yuan Chen Dushyant Dudhagara |
| author_sort | Bhumi Javia |
| collection | DOAJ |
| description | L-methioninase is an enzyme that has recently gained significant interest in the scientific community because of its potential as a targeted therapy for cancer. This study aims to isolate and identify extremophilic bacteria that could produce L-methioninase and to access the enzymatic potential of isolated bacteria under stress conditions, specifically in agro-industrial waste. In this study, a rare marine bacterium, <i>Alcaligenes aquatilis</i> BJ-1, exhibited the highest specific activity of 4.61 U/mg at an optimum pH of 8.3. The L-methioninase was purified 4.3-fold and 7.15-fold by acetone precipitation and Sephadex G-100 gel filtration chromatography, which revealed a molecular weight of 46 kDa. In addition, agriculture waste materials such as cottonseed oil cake had the highest L-methioninase production. Moreover, <i>A. aquatilis</i> BJ-1 can tolerate and produce enzymes in the presence of 10% NaCl, 6% KCl, and 4% MgSO<sub>4</sub>. Similarly, substrates such as L-asparagine, L-glutamine, L-alanine, and L-tyrosine were found suitable to increase enzyme production. The strain produced L-methioninase in the presence of various heavy metals. Maximum enzyme activity was found in Zn<sup>2+</sup> at 0.1% (2.52 U/mL), Li<sup>2+</sup> at 0.03% (2.90 U/mL), and Ni<sup>2+</sup> at 0.01% (2.78 U/mL), as compared to the control (2.23 U/mL) without metal. Enzyme production was also observed at a high temperature (60 °C), with the produced enzymes possessing antioxidant properties. In addition, no hemolytic activity was observed. The results indicate that <i>A. aquatilis</i> BJ-1 is an appropriate bacterium for metal bioremediation procedures in unfavorable circumstances. |
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| issn | 2036-7481 |
| language | English |
| last_indexed | 2024-03-10T22:27:58Z |
| publishDate | 2023-07-01 |
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| spelling | doaj.art-6c091fa3f4544096bdb9273d104354252023-11-19T11:58:12ZengMDPI AGMicrobiology Research2036-74812023-07-0114395997610.3390/microbiolres14030066Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial WasteBhumi Javia0Megha Gadhvi1Suhas Vyas2Pravin Dudhagara3Douglas J. H. Shyu4Yih-Yuan Chen5Dushyant Dudhagara6Department of Life Sciences, Bhakta Kavi Narsinh Mehta University, Khadiya, Junagadh 362263, Gujarat, IndiaDepartment of Life Sciences, Bhakta Kavi Narsinh Mehta University, Khadiya, Junagadh 362263, Gujarat, IndiaDepartment of Life Sciences, Bhakta Kavi Narsinh Mehta University, Khadiya, Junagadh 362263, Gujarat, IndiaDepartment of Biosciences (UGC-SAP-II & DST-FIST-I), Veer Narmad South Gujarat University, Surat 395007, Gujarat, IndiaDepartment of Biological Science and Technology, National Pingtung University of Science and Technology, Neipu, Pingtung 912301, TaiwanDepartment of Biochemical Science and Technology, National Chiayi University, Chiayi City 600355, TaiwanDepartment of Life Sciences, Bhakta Kavi Narsinh Mehta University, Khadiya, Junagadh 362263, Gujarat, IndiaL-methioninase is an enzyme that has recently gained significant interest in the scientific community because of its potential as a targeted therapy for cancer. This study aims to isolate and identify extremophilic bacteria that could produce L-methioninase and to access the enzymatic potential of isolated bacteria under stress conditions, specifically in agro-industrial waste. In this study, a rare marine bacterium, <i>Alcaligenes aquatilis</i> BJ-1, exhibited the highest specific activity of 4.61 U/mg at an optimum pH of 8.3. The L-methioninase was purified 4.3-fold and 7.15-fold by acetone precipitation and Sephadex G-100 gel filtration chromatography, which revealed a molecular weight of 46 kDa. In addition, agriculture waste materials such as cottonseed oil cake had the highest L-methioninase production. Moreover, <i>A. aquatilis</i> BJ-1 can tolerate and produce enzymes in the presence of 10% NaCl, 6% KCl, and 4% MgSO<sub>4</sub>. Similarly, substrates such as L-asparagine, L-glutamine, L-alanine, and L-tyrosine were found suitable to increase enzyme production. The strain produced L-methioninase in the presence of various heavy metals. Maximum enzyme activity was found in Zn<sup>2+</sup> at 0.1% (2.52 U/mL), Li<sup>2+</sup> at 0.03% (2.90 U/mL), and Ni<sup>2+</sup> at 0.01% (2.78 U/mL), as compared to the control (2.23 U/mL) without metal. Enzyme production was also observed at a high temperature (60 °C), with the produced enzymes possessing antioxidant properties. In addition, no hemolytic activity was observed. The results indicate that <i>A. aquatilis</i> BJ-1 is an appropriate bacterium for metal bioremediation procedures in unfavorable circumstances.https://www.mdpi.com/2036-7481/14/3/66agro-industrial waste<i>Alcaligenes aquatilis</i>L-methioninasethermostable |
| spellingShingle | Bhumi Javia Megha Gadhvi Suhas Vyas Pravin Dudhagara Douglas J. H. Shyu Yih-Yuan Chen Dushyant Dudhagara Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste Microbiology Research agro-industrial waste <i>Alcaligenes aquatilis</i> L-methioninase thermostable |
| title | Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste |
| title_full | Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste |
| title_fullStr | Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste |
| title_full_unstemmed | Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste |
| title_short | Bioprospecting of a Thermostable L-Methioninase from <i>Alcaligenes aquatilis</i> BJ-1 in Agro-Industrial Waste |
| title_sort | bioprospecting of a thermostable l methioninase from i alcaligenes aquatilis i bj 1 in agro industrial waste |
| topic | agro-industrial waste <i>Alcaligenes aquatilis</i> L-methioninase thermostable |
| url | https://www.mdpi.com/2036-7481/14/3/66 |
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